SHC4_HUMAN - dbPTM
SHC4_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SHC4_HUMAN
UniProt AC Q6S5L8
Protein Name SHC-transforming protein 4
Gene Name SHC4
Organism Homo sapiens (Human).
Sequence Length 630
Subcellular Localization Cell junction, synapse, postsynaptic cell membrane. Colocalized with MUSK at the neuromuscular junction..
Protein Description Activates both Ras-dependent and Ras-independent migratory pathways in melanomas. Contributes to the early phases of agrin-induced tyrosine phosphorylation of CHRNB1..
Protein Sequence MRERGQDSLAGLVLYVGLFGHPGMLHRAKYSRFRNESITSLDEGSSGGSVGNKGSPQPPHPALAPHLPTEDATLPSQESPTPLCTLIPRMASMKLANPATLLSLKNFCLGTKEVPRLKLQESRDPGSSGPSSPETSLSRSGTAPPPQQDLVGHRATALTPDSCPLPGPGEPTLRSRQDRHFLQHLLGMGMNYCVRYMGCVEVLQSMRSLDFGMRTQVTREAISRLCEAVPGANGAIKKRKPPVKFLSTVLGKSNLQFSGMNIKLTISTCSLTLMNLDNQQIIANHHMQSISFASGGDPDTTDYVAYVAKDPVNQRACHILECHNGMAQDVISTIGQAFELRFKQYLKNPSLNTSCESEEVHIDSHAEEREDHEYYNEIPGKQPPVGGVSDMRIKVQATEQMAYCPIQCEKLCYLPGNSKCSSVYENCLEQSRAIGNVHPRGVQSQRDTSLLKHTCRVDLFDDPCYINTQALQSTPGSAGNQRSAQPLGSPWHCGKAPETVQPGATAQPASSHSLPHIKQQLWSEECYHGKLSRKAAESLLVKDGDFLVRESATSPGQYVLSGLQGGQAKHLLLVDPEGKVRTKDHVFDNVGHLIRYHMDNSLPIISSGSEVSLKQPVRKDNNPALLHSNK
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
8PhosphorylationMRERGQDSLAGLVLY
CCCCCHHCHHHHHHH
16.54-
15PhosphorylationSLAGLVLYVGLFGHP
CHHHHHHHHHHHCCC
5.74-
37PhosphorylationYSRFRNESITSLDEG
HHHHCCCCCCCCCCC
34.4129507054
39PhosphorylationRFRNESITSLDEGSS
HHCCCCCCCCCCCCC
32.3028348404
40PhosphorylationFRNESITSLDEGSSG
HCCCCCCCCCCCCCC
31.9522617229
100PhosphorylationMKLANPATLLSLKNF
CCCCCHHHHHHHCHH
29.5024114839
103PhosphorylationANPATLLSLKNFCLG
CCHHHHHHHCHHHHC
40.1724505115
127PhosphorylationQESRDPGSSGPSSPE
CCCCCCCCCCCCCCC
37.1925850435
128PhosphorylationESRDPGSSGPSSPET
CCCCCCCCCCCCCCC
61.7125850435
131PhosphorylationDPGSSGPSSPETSLS
CCCCCCCCCCCCCCC
63.1525850435
132PhosphorylationPGSSGPSSPETSLSR
CCCCCCCCCCCCCCC
29.8629507054
135PhosphorylationSGPSSPETSLSRSGT
CCCCCCCCCCCCCCC
38.0525850435
136PhosphorylationGPSSPETSLSRSGTA
CCCCCCCCCCCCCCC
23.7625850435
159PhosphorylationGHRATALTPDSCPLP
CCCCEEECCCCCCCC
23.68-
196PhosphorylationGMNYCVRYMGCVEVL
CHHHHHHHHHHHHHH
4.2126503892
218PhosphorylationFGMRTQVTREAISRL
CCCCHHHHHHHHHHH
16.9926503892
374PhosphorylationEEREDHEYYNEIPGK
HHHCCHHHHHCCCCC
14.2622817900
375PhosphorylationEREDHEYYNEIPGKQ
HHCCHHHHHCCCCCC
11.8822817900
403PhosphorylationQATEQMAYCPIQCEK
EEECCCCCCCCCEEE
8.07-
413PhosphorylationIQCEKLCYLPGNSKC
CCEEEEEECCCCCCC
26.77-
424PhosphorylationNSKCSSVYENCLEQS
CCCCCHHHHHHHHHH
11.9025884760
448PhosphorylationGVQSQRDTSLLKHTC
CCCCHHHHHHHHCCC
24.38-
449PhosphorylationVQSQRDTSLLKHTCR
CCCHHHHHHHHCCCE
35.6724719451
465PhosphorylationDLFDDPCYINTQALQ
ECCCCCCEECHHHHH
11.5528152594
468PhosphorylationDDPCYINTQALQSTP
CCCCEECHHHHHCCC
12.9828152594
473PhosphorylationINTQALQSTPGSAGN
ECHHHHHCCCCCCCC
37.10-
489PhosphorylationRSAQPLGSPWHCGKA
CCCCCCCCCCCCCCC
32.2828555341
505PhosphorylationETVQPGATAQPASSH
CCCCCCCCCCCCCCC
31.5727251275
510PhosphorylationGATAQPASSHSLPHI
CCCCCCCCCCCCHHH
34.9527251275
511PhosphorylationATAQPASSHSLPHIK
CCCCCCCCCCCHHHH
21.1427251275
513PhosphorylationAQPASSHSLPHIKQQ
CCCCCCCCCHHHHHH
45.6127251275
523PhosphorylationHIKQQLWSEECYHGK
HHHHHHHCCHHHCCH
31.9126270265
527PhosphorylationQLWSEECYHGKLSRK
HHHCCHHHCCHHCHH
19.5226270265
532PhosphorylationECYHGKLSRKAAESL
HHHCCHHCHHHHHHH
34.9126270265
534AcetylationYHGKLSRKAAESLLV
HCCHHCHHHHHHHEE
48.888082881
538PhosphorylationLSRKAAESLLVKDGD
HCHHHHHHHEECCCC
23.44-
542AcetylationAAESLLVKDGDFLVR
HHHHHEECCCCEEEE
56.838082891
569AcetylationGLQGGQAKHLLLVDP
CCCCCCCEEEEEECC
27.228082901
596PhosphorylationNVGHLIRYHMDNSLP
CHHHHHHHHCCCCCC
8.42-
601PhosphorylationIRYHMDNSLPIISSG
HHHHCCCCCCEECCC
31.1227251275
606PhosphorylationDNSLPIISSGSEVSL
CCCCCEECCCCCEEC
29.39-
609PhosphorylationLPIISSGSEVSLKQP
CCEECCCCCEECCCC
36.45-
612PhosphorylationISSGSEVSLKQPVRK
ECCCCCEECCCCCCC
26.29-
628PhosphorylationNNPALLHSNK-----
CCCCCCCCCC-----
46.41-

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
159TPhosphorylationKinaseERK2P28482
PSP

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SHC4_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of SHC4_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
EGFR_HUMANEGFRphysical
24430869
GRB2_HUMANGRB2physical
24430869
NBEA_HUMANNBEAphysical
28514442
GARE1_HUMANGAREMphysical
28514442
IKKA_HUMANCHUKphysical
28514442
DCAM_HUMANAMD1physical
28514442
SHC3_HUMANSHC3physical
28514442

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SHC4_HUMAN

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Related Literatures of Post-Translational Modification

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